PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
23071334-5	2012	We have determined the crystal structure of human PRMT5 in complex with MEP50 (methylosome protein 50), bound to an S-adenosylmethionine analog and a peptide substrate derived from histone H4.	S-Adenosylmethionine	116-136	WD repeat domain 77	Homo sapiens	72-77	
29154828-0	2018	Interaction assessments of the first S-adenosylmethionine competitive inhibitor and the essential interacting partner methylosome protein 50 with protein arginine methyltransferase 5 by combined computational methods.	S-Adenosylmethionine	39-57	WD repeat domain 77	Homo sapiens	118-140	
28271477-4	2017	The structure of the 453 kDa heterooctameric PRMT5:MEP50 complex bound to an S-adenosylmethionine analog and a substrate peptide provides valuable insights into this intriguing target.	S-Adenosylmethionine	79-97	WD repeat domain 77	Homo sapiens	51-56	
23071334-5	2012	We have determined the crystal structure of human PRMT5 in complex with MEP50 (methylosome protein 50), bound to an S-adenosylmethionine analog and a peptide substrate derived from histone H4.	S-Adenosylmethionine	116-136	WD repeat domain 77	Homo sapiens	79-101